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Neuropeptide Y1 subtype pharmacology of a recombinantly expressed neuropeptide receptor

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Sprengel,  Rolf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society;
Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Krause, J., Eva, C., Seeburg, P. H., & Sprengel, R. (1992). Neuropeptide Y1 subtype pharmacology of a recombinantly expressed neuropeptide receptor. Molecular Pharmacology, 41(5), 817-821. Retrieved from http://molpharm.aspetjournals.org/content/41/5/817.


Zitierlink: http://hdl.handle.net/21.11116/0000-0000-6036-7
Zusammenfassung
Neuropeptide Y (NPY) is an important central and peripheral modulator of neural and endocrine functions. This neuropeptide interacts with at least two pharmacologically distinct receptors, termed Y1 and Y2. At Y1 receptors, the NPY analog [Leu31,Pro34] NPY, but not the carboxyl-terminal fragment NPY-(18-36), displaces radiolabeled NPY and the sequence-related peptide YY, whereas Y2 receptors exhibit the opposite selectivity. We have used cultured mammalian 293 cells for the high level transient expression of a previously cloned putative neuropeptide receptor of rat brain. We report that this receptor displays the ligand binding properties and selectivity of a Y1 receptor, with a single high affinity site for 125I-NPY (Kd, 0.7 +/- 0.2 nM). The functionality of the recombinantly expressed receptor was demonstrated by an inhibition of adenylyl cyclase and a concomitant mobilization of intracellular Ca2+.